5U0C

Structure of Zika virus NS5 RNA polymerase domain

Summary for 5U0C

• Entry DOI: 10.2210/pdb5u0c/pdb
• Descriptor: NS5 RNA polymerase domain, ZINC ION (2 entities in total)
• Functional Keywords: rna polymerase, transferase
• Biological source: Zika virus (strain Mr 766) (ZIKV)
• Cellular location: Protein C: Virion . Peptide pr: Secreted . Small envelope protein M: Virion membrane ; Multi-pass membrane protein . Envelope protein E: Virion membrane ; Single-pass membrane protein . Non-structural protein 1: Secreted . Non-structural protein 2A: Host endoplasmic reticulum membrane ; Multi- pass membrane protein . Serine protease subunit NS2B: Host endoplasmic reticulum membrane ; Peripheral membrane protein ; Cytoplasmic side . Serine protease NS3: Host endoplasmic reticulum membrane ; Peripheral membrane protein ; Cytoplasmic side . Non-structural protein 4A: Host endoplasmic reticulum membrane ; Multi- pass membrane protein . Non-structural protein 4B: Host endoplasmic reticulum membrane ; Multi- pass membrane protein . RNA-directed RNA polymerase NS5: Host endoplasmic reticulum membrane ; Peripheral membrane protein ; Cytoplasmic side : Q32ZE1
• Total number of polymer chains: 8
• Total formula weight: 591951.17

Authors

Zhao, B.,Du, F. (deposition date: 2016-11-23, release date: 2017-03-29, Last modification date: 2023-10-04)

Primary citation

Zhao, B.,Yi, G.,Du, F.,Chuang, Y.C.,Vaughan, R.C.,Sankaran, B.,Kao, C.C.,Li, P.
Structure and function of the Zika virus full-length NS5 protein.
Nat Commun, 8:14762-14762, 2017

PubMed Abstract: The recent outbreak of Zika virus (ZIKV) has infected over 1 million people in over 30 countries. ZIKV replicates its RNA genome using virally encoded replication proteins. Nonstructural protein 5 (NS5) contains a methyltransferase for RNA capping and a polymerase for viral RNA synthesis. Here we report the crystal structures of full-length NS5 and its polymerase domain at 3.0 Å resolution. The NS5 structure has striking similarities to the NS5 protein of the related Japanese encephalitis virus. The methyltransferase contains in-line pockets for substrate binding and the active site. Key residues in the polymerase are located in similar positions to those of the initiation complex for the hepatitis C virus polymerase. The polymerase conformation is affected by the methyltransferase, which enables a more efficiently elongation of RNA synthesis in vitro. Overall, our results will contribute to future studies on ZIKV infection and the development of inhibitors of ZIKV replication.

PubMed: 28345656
DOI: 10.1038/ncomms14762

Experimental method

X-RAY DIFFRACTION (3 Å)